LIG8_PHACH
ID LIG8_PHACH Reviewed; 372 AA.
AC P06181;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Ligninase H8;
DE EC=1.11.1.14 {ECO:0000269|PubMed:16593451, ECO:0000269|PubMed:2303054};
DE AltName: Full=Diarylpropane peroxidase;
DE AltName: Full=Lignin peroxidase {ECO:0000303|PubMed:16593451};
DE Flags: Precursor;
GN Name=LPOA;
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=3561490; DOI=10.1038/326520a0;
RA Tien M., Tu C.-P.D.;
RT "Cloning and sequencing of a cDNA for a ligninase from Phanerochaete
RT chrysosporium.";
RL Nature 326:520-523(1987).
RN [2]
RP ERRATUM OF PUBMED:3561490, AND SEQUENCE REVISION.
RA Tien M., Tu C.-P.D.;
RL Nature 328:742-742(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 29-48.
RX PubMed=3240864; DOI=10.1016/0378-1119(88)90111-4;
RA Walther L., Kaelin M., Reiser J., Suter F., Fritsche B., Saloheimo M.,
RA Leisola M., Teeri T., Knowles J.K.C., Fiechter A.;
RT "Molecular analysis of a Phanerochaete chrysosporium lignin peroxidase
RT gene.";
RL Gene 70:127-137(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=3344218; DOI=10.1093/nar/16.3.1219;
RA Smith T.L., Schalch H., Gaskell J., Covert S., Cullan D.;
RT "Nucleotide sequence of a ligninase gene from Phanerochaete
RT chrysosporium.";
RL Nucleic Acids Res. 16:1219-1219(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2474293; DOI=10.1016/0006-291x(89)92363-2;
RA Andrawis A., Pease E.A., Kuan I., Holzbaur E., Tien M.;
RT "Characterization of two lignin peroxidase clones from Phanerochaete
RT chrysosporium.";
RL Biochem. Biophys. Res. Commun. 162:673-680(1989).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1.
RX PubMed=2844176; DOI=10.1016/s0006-291x(88)80541-2;
RA Holzbaur E.L.F., Tien M.;
RT "Structure and regulation of a lignin peroxidase gene from Phanerochaete
RT chrysosporium.";
RL Biochem. Biophys. Res. Commun. 155:626-633(1988).
RN [7]
RP PROTEIN SEQUENCE OF 29-58, FUNCTION, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=2303054; DOI=10.1111/j.1432-1033.1990.tb15333.x;
RA Glumoff T., Harvey P.J., Molinari S., Goble M., Frank G., Palmer J.M.,
RA Smit J.D.G., Leisola M.S.A.;
RT "Lignin peroxidase from Phanerochaete chrysosporium. Molecular and kinetic
RT characterization of isozymes.";
RL Eur. J. Biochem. 187:515-520(1990).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP CHARACTERIZATION.
RX PubMed=16593451; DOI=10.1073/pnas.81.8.2280;
RA Tien M., Kirk T.K.;
RT "Lignin-degrading enzyme from Phanerochaete chrysosporium: purification,
RT characterization, and catalytic properties of a unique H2O2-requiring
RT oxygenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:2280-2284(1984).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=11607355; DOI=10.1073/pnas.90.2.750;
RA Edwards S.L., Raag R., Wariishi H., Gold M.H., Poulos T.L.;
RT "Crystal structure of lignin peroxidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:750-754(1993).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RC STRAIN=ATCC 24725 / DSM 6909 / CBS 481.73 / BCRC 36200 / NRRL 6361 / VKM
RC F-1767;
RX PubMed=9636023; DOI=10.1021/bi9727186;
RA Blodig W., Doyle W.A., Smith A.T., Winterhalter K.H., Choinowski T.,
RA Piontek K.;
RT "Autocatalytic formation of a hydroxy group at C beta of Trp171 in lignin
RT peroxidase.";
RL Biochemistry 37:8832-8838(1998).
CC -!- FUNCTION: Depolymerization of lignin. Catalyzes the C(alpha)-C(beta)
CC cleavage of the propyl side chains of lignin.
CC {ECO:0000269|PubMed:16593451, ECO:0000269|PubMed:2303054}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol +
CC H2O2 = 3,4-dimethoxybenzaldehyde + glycolaldehyde + guaiacol + H2O;
CC Xref=Rhea:RHEA:48004, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17071, ChEBI:CHEBI:17098, ChEBI:CHEBI:28591,
CC ChEBI:CHEBI:86963; EC=1.11.1.14;
CC Evidence={ECO:0000269|PubMed:16593451, ECO:0000269|PubMed:2303054};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 (3,4-dimethoxyphenyl)methanol + H2O2 = 2 (3,4-
CC dimethoxyphenyl)methanol radical + 2 H2O; Xref=Rhea:RHEA:30271,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:62150,
CC ChEBI:CHEBI:88143; EC=1.11.1.14;
CC Evidence={ECO:0000269|PubMed:16593451, ECO:0000269|PubMed:2303054};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 2 calcium ions per subunit.;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000269|PubMed:16593451};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
CC {ECO:0000269|PubMed:16593451};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=130 uM for H(2)O(2) {ECO:0000269|PubMed:2303054};
CC KM=116 uM for (3,4-dimethoxyphenyl)methanol
CC {ECO:0000269|PubMed:3240864};
CC KM=30 uM for H(2)O(2) {ECO:0000269|PubMed:16593451};
CC pH dependence:
CC Optimum pH is 3. {ECO:0000269|PubMed:16593451,
CC ECO:0000269|PubMed:2303054};
CC -!- PATHWAY: Secondary metabolite metabolism; lignin degradation.
CC -!- DEVELOPMENTAL STAGE: Ligninases are expressed during secondary
CC metabolism, and are triggered by nutrient limitation.
CC -!- SIMILARITY: Belongs to the peroxidase family. Ligninase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33740.1; Type=Erroneous translation; Evidence={ECO:0000305};
CC Sequence=CAA68373.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M37701; AAA33740.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Y00262; CAA68373.1; ALT_FRAME; mRNA.
DR EMBL; M21913; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M27401; AAA53109.1; -; Genomic_DNA.
DR EMBL; M27884; AAB00798.1; -; Genomic_DNA.
DR PIR; A27817; A27817.
DR PIR; A32322; A32322.
DR PIR; A43638; A43638.
DR PIR; B32322; B32322.
DR PIR; JT0402; JT0402.
DR PIR; PS0010; PS0010.
DR PIR; S01028; S01028.
DR PIR; S08202; S08202.
DR PIR; S69246; S69246.
DR PDB; 1B80; X-ray; 1.73 A; A/B=22-372.
DR PDB; 1B82; X-ray; 1.80 A; A/B=22-372.
DR PDB; 1B85; X-ray; 1.85 A; A/B=22-372.
DR PDB; 6A6Q; X-ray; 1.67 A; A=22-372.
DR PDB; 6ISS; X-ray; 1.53 A; A/G=22-372.
DR PDBsum; 1B80; -.
DR PDBsum; 1B82; -.
DR PDBsum; 1B85; -.
DR PDBsum; 6A6Q; -.
DR PDBsum; 6ISS; -.
DR AlphaFoldDB; P06181; -.
DR SMR; P06181; -.
DR CAZy; AA2; Auxiliary Activities 2.
DR CLAE; LPO2H_PHACH; -.
DR PeroxiBase; 2412; PcLiP01_RP78.
DR KEGG; ag:AAA33740; -.
DR VEuPathDB; FungiDB:AGR57_14163; -.
DR BioCyc; MetaCyc:MON-14338; -.
DR BRENDA; 1.11.1.14; 1380.
DR UniPathway; UPA00892; -.
DR EvolutionaryTrace; P06181; -.
DR GO; GO:0016690; F:diarylpropane peroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046274; P:lignin catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00692; ligninase; 1.
DR InterPro; IPR044831; Ccp1-like.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR001621; Ligninase.
DR InterPro; IPR024589; Ligninase_C.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR31356; PTHR31356; 1.
DR Pfam; PF00141; peroxidase; 1.
DR Pfam; PF11895; Peroxidase_ext; 1.
DR PRINTS; PR00462; LIGNINASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Heme;
KW Hydrogen peroxide; Iron; Lignin degradation; Metal-binding; Oxidoreductase;
KW Peroxidase; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..28
FT /evidence="ECO:0000269|PubMed:2303054"
FT /id="PRO_0000023760"
FT CHAIN 29..372
FT /note="Ligninase H8"
FT /id="PRO_0000023761"
FT REGION 350..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 75
FT /note="Proton acceptor"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 204
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT SITE 71
FT /note="Transition state stabilizer"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..43
FT DISULFID 42..313
FT DISULFID 62..148
FT DISULFID 277..345
FT VARIANT 15
FT /note="L -> S"
FT VARIANT 142
FT /note="R -> A"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:6ISS"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:6ISS"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6ISS"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 133..146
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 194..198
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:6ISS"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:6ISS"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:6ISS"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:1B80"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:6ISS"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 276..280
FT /evidence="ECO:0007829|PDB:6ISS"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 286..301
FT /evidence="ECO:0007829|PDB:6ISS"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:6ISS"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:6ISS"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:6ISS"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:6ISS"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:6ISS"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:6ISS"
SQ SEQUENCE 372 AA; 39686 MW; E6ABA9FD48428FCC CRC64;
MAFKQLFAAI SLALLLSAAN AAAVIEKRAT CSNGKTVGDA SCCAWFDVLD DIQQNLFHGG
QCGAEAHESI RLVFHDSIAI SPAMEAQGKF GGGGADGSIM IFDDIETAFH PNIGLDEIVK
LQKPFVQKHG VTPGDFIAFA GRVALSNCPG APQMNFFTGR APATQPAPDG LVPEPFHTVD
QIINRVNDAG EFDELELVWM LSAHSVAAVN DVDPTVQGLP FDSTPGIFDS QFFVETQLRG
TAFPGSGGNQ GEVESPLPGE IRIQSDHTIA RDSRTACEWQ SFVNNQSKLV DDFQFIFLAL
TQLGQDPNAM TDCSDVIPQS KPIPGNLPFS FFPAGKTIKD VEQACAETPF PTLTTLPGPE
TSVQRIPPPP GA
